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Literature summary extracted from

  • Fisher, A.B.
    Peroxiredoxin 6: A bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities (2010), Antioxid. Redox Signal., 15, 831-844.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.27 DNA and amino acid sequence determination, analysis, and comparison Homo sapiens
1.11.1.27 DNA and amino acid sequence determination, analysis, and comparison Rattus norvegicus
1.11.1.27 DNA and amino acid sequence determination, analysis, and comparison Bos taurus
1.11.1.27 Prdx6 gene, DNA and amino acid sequence determination and analysis, comprises 5 exons and 4 introns and is located on chromosome 1, mapped to a 0.66 cM interval between D1Mit 159 and D1Mit 398, sequence comparison Mus musculus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.27 X-ray diffraction structure determination and analysis at 2.0 A resolution Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.1.27 Mercaptosuccinate a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected Bos taurus
1.11.1.27 Mercaptosuccinate a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected Homo sapiens
1.11.1.27 Mercaptosuccinate a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected Mus musculus
1.11.1.27 Mercaptosuccinate a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected Rattus norvegicus
1.11.1.27 MJ33 a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity Bos taurus
1.11.1.27 MJ33 a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity Homo sapiens
1.11.1.27 MJ33 a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity Mus musculus
1.11.1.27 MJ33 a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity Rattus norvegicus
1.11.1.27 additional information serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity Bos taurus
1.11.1.27 additional information serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity Homo sapiens
1.11.1.27 additional information serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity Mus musculus
1.11.1.27 additional information serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.27 cytosol cytosolic Prdx6 could bind to and reduce peroxidized membrane phospholipids followed by its dissociation from the membrane and return to the cytosolic compartment Mus musculus 5829
-
1.11.1.27 cytosol cytosolic Prdx6 could bind to and reduce peroxidized membrane phospholipids followed by its dissociation from the membrane and return to the cytosolic compartment Homo sapiens 5829
-
1.11.1.27 cytosol cytosolic Prdx6 could bind to and reduce peroxidized membrane phospholipids followed by its dissociation from the membrane and return to the cytosolic compartment Rattus norvegicus 5829
-
1.11.1.27 cytosol cytosolic Prdx6 could bind to and reduce peroxidized membrane phospholipids followed by its dissociation from the membrane and return to the cytosolic compartment Bos taurus 5829
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.27 25100
-
 x * 25100, about, sequence calculation, x * 26000-29000, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.1.27 2 GSH + ROOH Mus musculus glutathione is the primary native reductant GSSG + H2O + ROH
-
 ?
1.11.1.27 2 GSH + ROOH Homo sapiens glutathione is the primary native reductant GSSG + H2O + ROH
-
 ?
1.11.1.27 2 GSH + ROOH Rattus norvegicus glutathione is the primary native reductant GSSG + H2O + ROH
-
 ?
1.11.1.27 2 GSH + ROOH Bos taurus glutathione is the primary native reductant GSSG + H2O + ROH
-
 ?
1.11.1.27 additional information Mus musculus the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview ?
-
 ?
1.11.1.27 additional information Homo sapiens the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview ?
-
 ?
1.11.1.27 additional information Rattus norvegicus the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview ?
-
 ?
1.11.1.27 additional information Bos taurus the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.27 Bos taurus
-
-
-
1.11.1.27 Homo sapiens
-
-
-
1.11.1.27 Mus musculus
-
-
-
1.11.1.27 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.11.1.27 phosphoprotein MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6 Mus musculus
1.11.1.27 phosphoprotein MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6 Homo sapiens
1.11.1.27 phosphoprotein MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6 Rattus norvegicus
1.11.1.27 phosphoprotein MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.1.27 brain
-
 Mus musculus
-
1.11.1.27 brain
-
 Homo sapiens
-
1.11.1.27 brain
-
 Rattus norvegicus
-
1.11.1.27 brain
-
 Bos taurus
-
1.11.1.27 epidermis
-
 Mus musculus
-
1.11.1.27 epidermis
-
 Homo sapiens
-
1.11.1.27 epidermis
-
 Rattus norvegicus
-
1.11.1.27 epidermis
-
 Bos taurus
-
1.11.1.27 epithelium
-
 Mus musculus
-
1.11.1.27 epithelium
-
 Homo sapiens
-
1.11.1.27 epithelium
-
 Rattus norvegicus
-
1.11.1.27 epithelium
-
 Bos taurus
-
1.11.1.27 eye ciliary body Bos taurus
-
1.11.1.27 kidney
-
 Mus musculus
-
1.11.1.27 kidney
-
 Homo sapiens
-
1.11.1.27 kidney
-
 Rattus norvegicus
-
1.11.1.27 kidney
-
 Bos taurus
-
1.11.1.27 liver
-
 Mus musculus
-
1.11.1.27 liver
-
 Homo sapiens
-
1.11.1.27 liver
-
 Rattus norvegicus
-
1.11.1.27 liver
-
 Bos taurus
-
1.11.1.27 lung especially in type II alveolar epithelial cells and bronchiolar Clara cells Mus musculus
-
1.11.1.27 lung especially in type II alveolar epithelial cells and bronchiolar Clara cells Homo sapiens
-
1.11.1.27 lung especially in type II alveolar epithelial cells and bronchiolar Clara cells Rattus norvegicus
-
1.11.1.27 lung especially in type II alveolar epithelial cells and bronchiolar Clara cells Bos taurus
-
1.11.1.27 additional information within organs, expression of Prdx is greatest in epithelium such as apical regions of respiratory epithelium and skin epidermis, tissue distribution, overview Mus musculus
-
1.11.1.27 additional information within organs, expression of Prdx is greatest in epithelium such as apical regions of respiratory epithelium and skin epidermis, tissue distribution, overview Homo sapiens
-
1.11.1.27 additional information within organs, expression of Prdx is greatest in epithelium such as apical regions of respiratory epithelium and skin epidermis, tissue distribution, overview Rattus norvegicus
-
1.11.1.27 additional information within organs, expression of Prdx is greatest in epithelium such as apical regions of respiratory epithelium and skin epidermis, tissue distribution, overview Bos taurus
-
1.11.1.27 olfactory mucosa
-
 Rattus norvegicus
-
1.11.1.27 testis
-
 Mus musculus
-
1.11.1.27 testis
-
 Homo sapiens
-
1.11.1.27 testis
-
 Rattus norvegicus
-
1.11.1.27 testis
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.27 2 GSH + ROOH
-
 Mus musculus GSSG + H2O + ROH
-
 ?
1.11.1.27 2 GSH + ROOH
-
 Homo sapiens GSSG + H2O + ROH
-
 ?
1.11.1.27 2 GSH + ROOH
-
 Rattus norvegicus GSSG + H2O + ROH
-
 ?
1.11.1.27 2 GSH + ROOH
-
 Bos taurus GSSG + H2O + ROH
-
 ?
1.11.1.27 2 GSH + ROOH glutathione is the primary native reductant Mus musculus GSSG + H2O + ROH
-
 ?
1.11.1.27 2 GSH + ROOH glutathione is the primary native reductant Homo sapiens GSSG + H2O + ROH
-
 ?
1.11.1.27 2 GSH + ROOH glutathione is the primary native reductant Rattus norvegicus GSSG + H2O + ROH
-
 ?
1.11.1.27 2 GSH + ROOH glutathione is the primary native reductant Bos taurus GSSG + H2O + ROH
-
 ?
1.11.1.27 additional information the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview Mus musculus ?
-
 ?
1.11.1.27 additional information the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview Homo sapiens ?
-
 ?
1.11.1.27 additional information the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview Rattus norvegicus ?
-
 ?
1.11.1.27 additional information the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview Bos taurus ?
-
 ?
1.11.1.27 additional information DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities Mus musculus ?
-
 ?
1.11.1.27 additional information DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities Homo sapiens ?
-
 ?
1.11.1.27 additional information DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities Rattus norvegicus ?
-
 ?
1.11.1.27 additional information DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities Bos taurus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.1.27 ? x * 25100, about, sequence calculation, x * 26000-29000, SDS-PAGE Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.11.1.27 1-Cys Prdx
-
 Mus musculus
1.11.1.27 1-Cys Prdx
-
 Homo sapiens
1.11.1.27 1-Cys Prdx
-
 Rattus norvegicus
1.11.1.27 1-Cys Prdx
-
 Bos taurus
1.11.1.27 peroxiredoxin 6
-
 Mus musculus
1.11.1.27 peroxiredoxin 6
-
 Homo sapiens
1.11.1.27 peroxiredoxin 6
-
 Rattus norvegicus
1.11.1.27 peroxiredoxin 6
-
 Bos taurus
1.11.1.27 Prdx6 Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family Mus musculus
1.11.1.27 Prdx6 Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family Homo sapiens
1.11.1.27 Prdx6 Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family Rattus norvegicus
1.11.1.27 Prdx6 Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family Bos taurus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.11.1.27 Homo sapiens
-
-
 5.1

Expression

EC Number Organism Comment Expression
1.11.1.27 Mus musculus oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE up
1.11.1.27 Homo sapiens oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE up
1.11.1.27 Bos taurus oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE up
1.11.1.27 Rattus norvegicus transcription of Prdx6 message in dermal epithelium is induced by treatment with keratinocyte growth factor, a response of presumed importance related to wound healing, requiring ARE and Nrf2. Dexamethasone induces Prdx6 expression in adult lung cells and regulates transcription through its interaction with a glucocorticoid response element in the promoter region of the Prdx6 gene. Oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE up

General Information

EC Number General Information Comment Organism
1.11.1.27 additional information regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation Mus musculus
1.11.1.27 additional information regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation Homo sapiens
1.11.1.27 additional information regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation Rattus norvegicus
1.11.1.27 additional information regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation Bos taurus
1.11.1.27 physiological function Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis Mus musculus
1.11.1.27 physiological function Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis Homo sapiens
1.11.1.27 physiological function Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis Rattus norvegicus
1.11.1.27 physiological function Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis Bos taurus